Reference health

Pathological α-synuclein transmission initiated by binding lymphocyte-activation gene 3

https://doi.org/10.1126/science.aah3374
CiteStamped reference-health badge
50/50 checkable references clean · checked 2026-08-31

Every reference with a DOI in the deposited reference list resolved to a known work in Crossref or DataCite at the dated check, and none carried a retraction, withdrawal, or removal notice.

1 without a DOI — not checked. A reference deposited without a DOI is never matched by title or guessed at; it stays outside the checked set, and this line discloses that.

The 50 checked references that resolve
resolves10.1038/35081564
Alpha-synuclein and neurodegenerative diseases
resolves10.1038/nrneurol.2012.242
100 years of Lewy pathology
resolves10.1016/j.neuron.2006.09.026
Mechanisms of Parkinson's Disease Linked to Pathological α-Synuclein: New Targets for Drug Discovery
resolves10.1002/mds.26370
Alpha‐synuclein propagation: New insights from animal models
resolves10.1007/978-1-61779-551-0_23
Cell-to-Cell Transmission of α-Synuclein Aggregates
resolves10.1111/jnc.13449
Sorting out release, uptake and processing of alpha‐synuclein during prion‐like spread of pathology
resolves10.1016/S0197-4580(02)00065-9
Staging of brain pathology related to sporadic Parkinson’s disease
resolves10.1111/nan.12298
Review: Sporadic Parkinson's disease: development and distribution of<i>α</i>‐synuclein pathology
resolves10.1038/nm1747
Lewy body–like pathology in long-term embryonic nigral transplants in Parkinson's disease
resolves10.1038/nm1746
Lewy bodies in grafted neurons in subjects with Parkinson's disease suggest host-to-graft disease propagation
resolves10.1146/annurev-neuro-071714-033828
Neurodegenerative Diseases: Expanding the Prion Concept
resolves10.1038/nature12481
Self-propagation of pathogenic protein aggregates in neurodegenerative diseases
resolves10.1016/j.neuron.2011.08.033
Exogenous α-Synuclein Fibrils Induce Lewy Body Pathology Leading to Synaptic Dysfunction and Neuron Death
resolves10.1126/science.1227157
Pathological α-Synuclein Transmission Initiates Parkinson-like Neurodegeneration in Nontransgenic Mice
resolves10.1111/j.1600-0854.2008.00853.x
α‐Synuclein and Polyunsaturated Fatty Acids Promote Clathrin‐Mediated Endocytosis and Synaptic Vesicle Recycling
resolves10.1111/j.1471-4159.2011.07460.x
α‐Synuclein promotes clathrin‐mediated NMDA receptor endocytosis and attenuates NMDA‐induced dopaminergic cell death
resolves10.1016/j.celrep.2015.12.075
Mesenchymal Stem Cells Inhibit Transmission of α-Synuclein by Modulating Clathrin-Mediated Endocytosis in a Parkinsonian Model
resolves10.1038/nprot.2014.143
Addition of exogenous α-synuclein preformed fibrils to primary neuronal cultures to seed recruitment of endogenous α-synuclein to Lewy body and Lewy neurite–like aggregates
resolves10.1016/0092-8674(94)90408-1
Identification and cloning of ELF-1, a developmentally expressed ligand for the Mek4 and Sek receptor tyrosine kinases
resolves10.1038/nature07761
Cellular prion protein mediates impairment of synaptic plasticity by amyloid-β oligomers
resolves10.1073/pnas.132197599
Human α-synuclein-harboring familial Parkinson's disease-linked Ala-53 → Thr mutation causes neurodegenerative disease with α-synuclein aggregation in transgenic mice
resolves10.1073/pnas.94.11.5744
Characterization of the major histocompatibility complex class II binding site on LAG-3 protein
resolves10.1021/cr900249z
Fluorescent Indicators for Intracellular pH
resolves10.1038/emboj.2011.286
Endosome maturation
resolves10.1074/jbc.270.22.13503
EEA1, an Early Endosome-Associated Protein.
resolves10.1371/journal.pone.0091465
Subcellular Fractionation and Localization Studies Reveal a Direct Interaction of the Fragile X Mental Retardation Protein (FMRP) with Nucleolin
resolves10.1242/jcs.180737
Ca2+ is a key factor in α-synuclein-induced neurotoxicity
resolves10.1111/j.1471-4159.2009.06411.x
α‐Synuclein modulation of Ca<sup>2+</sup>signaling in human neuroblastoma (SH‐SY5Y) cells
resolves10.1016/j.neurobiolaging.2013.06.006
Deregulation of calcium homeostasis mediates secreted α–synuclein-induced neurotoxicity
resolves10.1016/j.mcn.2010.12.004
Raised calcium promotes α-synuclein aggregate formation
resolves10.15252/embj.201591397
α‐synuclein assemblies sequester neuronal α3‐Na+/K+‐ATPase and impair Na+ gradient
resolves10.1002/1521-4141(200208)32:8<2255::AID-IMMU2255>3.0.CO;2-A
Phenotypic analysis of the murine CD4-related glycoprotein, CD223 (LAG-3)
resolves10.1002/eji.200939874
Differential subcellular localization of the regulatory T‐cell protein LAG‐3 and the coreceptor CD4
resolves10.1126/science.272.5260.405
Independent Modes of Natural Killing Distinguished in Mice Lacking <b> <i>Lag3</i> </b>
resolves10.1084/jem.20112457
Intracerebral inoculation of pathological α-synuclein initiates a rapidly progressive neurodegenerative α-synucleinopathy in mice
resolves10.1038/srep04874
The c-Abl inhibitor, Nilotinib, protects dopaminergic neurons in a preclinical animal model of Parkinson's disease
resolves10.1038/ncomms2534
Neuron-released oligomeric α-synuclein is an endogenous agonist of TLR2 for paracrine activation of microglia
resolves10.1073/pnas.1301440110
Heparan sulfate proteoglycans mediate internalization and propagation of specific proteopathic seeds
resolves10.1126/science.290.5499.2155
Functional Requirement for Class I MHC in CNS Development and Plasticity
resolves10.1016/j.neuron.2009.09.044
MHC Class I: An Unexpected Role in Neuronal Plasticity
resolves10.1002/glia.1108
Control of glial immune function by neurons
resolves10.1016/j.immuni.2016.05.001
Lag-3, Tim-3, and TIGIT: Co-inhibitory Receptors with Specialized Functions in Immune Regulation
resolves10.1038/ncb3372
Unconventional secretion of misfolded proteins promotes adaptation to proteasome dysfunction in mammalian cells
resolves10.1074/jbc.M110.209296
Seeding of Normal Tau by Pathological Tau Conformers Drives Pathogenesis of Alzheimer-like Tangles
resolves10.1172/JCI66827
FcγRIIb mediates amyloid-β neurotoxicity and memory impairment in Alzheimer’s disease
resolves10.1523/JNEUROSCI.0302-15.2015
Fyn Kinase Regulates Microglial Neuroinflammatory Responses in Cell Culture and Animal Models of Parkinson's Disease
resolves10.1002/eji.200323382
The CD4‐related molecule, LAG‐3 (CD223), regulates the expansion of activated T cells
resolves10.1038/nm.2387
Iduna protects the brain from glutamate excitotoxicity and stroke by interfering with poly(ADP-ribose) polymer-induced cell death
resolves10.1523/JNEUROSCI.0864-14.2014
Inhibition of Adenylyl Cyclase Type 5 Prevents l-DOPA-Induced Dyskinesia in an Animal Model of Parkinson's Disease
resolves10.1016/j.bbr.2010.03.004
Behavioral phenotyping of mouse models of Parkinson's disease
The 1 reference without a DOI — listed, not checked
no DOI — not checkedChengH. J.FlanaganJ. G., Cloning and characterization of RTK ligands using receptor-alkaline phosphatase fusion proteins. Methods Mol. Biol. 124, 313–334 (2001).11100484
What this badge says. CiteStamped means the CHECKABLE references of this work were clean at the dated check: each resolved to a known work in a public registry, and none carried a retraction notice at that time. It says nothing about the quality, findings, or importance of the work itself, and nothing about references deposited without a DOI.

checked 2026-08-31 — re-checked daily as this page is visited; titles and statuses come from Crossref and DataCite and are not part of the signed record

Embed this badge

Both snippets point at the live badge image and link back to this page. The badge re-renders from the daily check, so an embed never goes stale by more than a day of visits.

<a href="https://citestamp.com/citestamped/10.1126/science.aah3374"><img src="https://citestamp.com/citestamped/10.1126/science.aah3374/badge.svg" alt="CiteStamped reference-health badge" width="460" height="64"></a>
[![CiteStamped reference-health badge](https://citestamp.com/citestamped/10.1126/science.aah3374/badge.svg)](https://citestamp.com/citestamped/10.1126/science.aah3374)